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| | <StructureSection load='4pzo' size='340' side='right'caption='[[4pzo]], [[Resolution|resolution]] 2.25Å' scene=''> | | <StructureSection load='4pzo' size='340' side='right'caption='[[4pzo]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4pzo]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PZO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PZO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4pzo]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PZO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PZO FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pzn|4pzn]]</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzo OCA], [https://pdbe.org/4pzo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pzo RCSB], [https://www.ebi.ac.uk/pdbsum/4pzo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pzo ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EDR3, PH3, PHC3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzo OCA], [http://pdbe.org/4pzo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pzo RCSB], [http://www.ebi.ac.uk/pdbsum/4pzo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pzo ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PHC3_HUMAN PHC3_HUMAN]] Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility.<ref>PMID:12167701</ref> | + | [https://www.uniprot.org/uniprot/PHC3_HUMAN PHC3_HUMAN] Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility.<ref>PMID:12167701</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hale, S M]] | + | [[Category: Hale SM]] |
| - | [[Category: Halloran, J]] | + | [[Category: Halloran J]] |
| - | [[Category: Hart, P J]] | + | [[Category: Hart PJ]] |
| - | [[Category: Junco, S E]] | + | [[Category: Junco SE]] |
| - | [[Category: Kaur, Y]] | + | [[Category: Kaur Y]] |
| - | [[Category: Kim, C A]] | + | [[Category: Kim CA]] |
| - | [[Category: Nanyes, D R]] | + | [[Category: Nanyes DR]] |
| - | [[Category: Patterson, N L]] | + | [[Category: Patterson NL]] |
| - | [[Category: Robinson, A K]] | + | [[Category: Robinson AK]] |
| - | [[Category: Shivarajpur, A]] | + | [[Category: Shivarajpur A]] |
| - | [[Category: Taylor, A B]] | + | [[Category: Taylor AB]] |
| - | [[Category: Chromatin]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Polycomb group]]
| + | |
| - | [[Category: Polymer]]
| + | |
| - | [[Category: Sam domain]]
| + | |
| Structural highlights
Function
PHC3_HUMAN Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility.[1]
Publication Abstract from PubMed
The self-association of sterile alpha motifs (SAMs) into a helical polymer architecture is a critical functional component of many different and diverse array of proteins. For the Drosophila Polycomb group (PcG) protein Polyhomeotic (Ph), its SAM polymerization serves as the structural foundation to cluster multiple PcG complexes, helping to maintain a silenced chromatin state. Ph SAM shares 64% sequence identity with its human ortholog, PHC3 SAM, and both SAMs polymerize. However, in the context of their larger protein regions, PHC3 SAM forms longer polymers compared to Ph SAM. Motivated to establish the precise structural basis for the differences, if any, between Ph and PHC3 SAM, we determined the crystal structure of the PHC3 SAM polymer. PHC3 SAM utilizes the same SAM-SAM interaction as the Ph SAM six-fold repeat polymer. Yet, PHC3 SAM polymerizes utilizing just five SAMs per turn of the helical polymer rather than the typical six per turn observed for all SAM polymers reported to date. Structural analysis suggested that malleability of the PHC3 SAM would allow formation of not just the five-fold repeat structure but possibly others. Indeed, a second PHC3 SAM polymer in a different crystal form forms a six-fold repeat polymer. These results suggest that the polymers formed by PHC3 SAM, and likely others, are quite dynamic. The functional consequence of the variable PHC3 SAM polymers may be to create different chromatin architectures. (c) Proteins 2014;. (c) 2014 Wiley Periodicals, Inc.
Multiple polymer architectures of human polyhomeotic homolog 3 (PHC3) SAM.,Nanyes DR, Junco SE, Taylor AB, Robinson AK, Patterson NL, Shivarajpur A, Halloran J, Hale SM, Kaur Y, Hart PJ, Kim CA Proteins. 2014 Jul 15. doi: 10.1002/prot.24645. PMID:25044168[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Levine SS, Weiss A, Erdjument-Bromage H, Shao Z, Tempst P, Kingston RE. The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans. Mol Cell Biol. 2002 Sep;22(17):6070-8. PMID:12167701
- ↑ Nanyes DR, Junco SE, Taylor AB, Robinson AK, Patterson NL, Shivarajpur A, Halloran J, Hale SM, Kaur Y, Hart PJ, Kim CA. Multiple polymer architectures of human polyhomeotic homolog 3 (PHC3) SAM. Proteins. 2014 Jul 15. doi: 10.1002/prot.24645. PMID:25044168 doi:http://dx.doi.org/10.1002/prot.24645
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